6xzc | pdb_00006xzc

CryoEM structure of the ring-shaped virulence factor EspB from Mycobacterium tuberculosis

spinqualitylabelsall models 6xzc, resolution 3.37Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6xzc is a 7 chain structure with sequence from Mycobacterium tuberculosis H37Rv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.37Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ESPB_MYCTU Publication Abstract from PubMed The EspB protein of Mycobacterium tuberculosis is a 60 kDa virulence factor, implicated in conjugation and exported by the ESX-1 system of which it may also be a component. Previous attempts to obtain high-resolution maps of EspB by cryo-electron microscopic examination of single particles have been thwarted by severe orientation bias of the particles. This was overcome by using detergent as a surfactant thereby allowing reconstruction of the EspB structure at 3.37 A resolution. The final structure revealed the N-terminal domain of EspB to be organized as a cylindrical heptamer with dimensions of 90 A x 90 A and a central channel of 45 A diameter whereas the C-terminal domain was unstructured. New atomic insight was obtained into the helical packing required for protomer interactions and the overall electrostatic potential. The external surface is electronegatively charged while the channel is lined with electropositive patches. EspB thus has many features of a pore-like transport protein that might allow the passage of an ESX-1 substrate such as the 35 A diameter EsxA-EsxB heterodimer or B-form DNA consistent with its proposed role in DNA uptake. High resolution CryoEM structure of the ring-shaped virulence factor EspB from Mycobacterium tuberculosis.,Piton J, Pojer F, Wakatsuki S, Gati C, Cole ST J Struct Biol X. 2020 Jul 2;4:100029. doi: 10.1016/j.yjsbx.2020.100029., eCollection 2020. PMID:32875288 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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